X-ray diffraction
1.99Å resolution

Crystal structure of the Lon-like protease MtaLonC in complex with lactacystin

Source organism: Meiothermus taiwanensis
Primary publication:
Structures of an ATP-independent Lon-like protease and its complexes with covalent inhibitors.
Acta Crystallogr. D Biol. Crystallogr. 69 1395-402 (2013)
PMID: 23897463

Function and Biology Details

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Endopeptidase La Chain: A
Molecule details ›
Chain: A
Length: 732 amino acids
Theoretical weight: 81.07 KDa
Source organism: Meiothermus taiwanensis
Expression system: Escherichia coli
  • Canonical: C9DRU9 (Residues: 1-719; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P6
Unit cell:
a: 115.987Å b: 115.987Å c: 135.054Å
α: 90° β: 90° γ: 120°
R R work R free
0.231 0.23 0.259
Expression system: Escherichia coli